2024
Tomosyns attenuate SNARE assembly and synaptic depression by binding to VAMP2-containing template complexes
Meijer M, Öttl M, Yang J, Subkhangulova A, Kumar A, Feng Z, van Voorst T, Groffen A, van Weering J, Zhang Y, Verhage M. Tomosyns attenuate SNARE assembly and synaptic depression by binding to VAMP2-containing template complexes. Nature Communications 2024, 15: 2652. PMID: 38531902, PMCID: PMC10965968, DOI: 10.1038/s41467-024-46828-1.Peer-Reviewed Original ResearchConceptsSynaptobrevin-2/VAMP2SNARE assemblySNARE motifC-terminal polybasic regionSNAP-25 bindingSNARE complex assemblyTemplate complexStructure-function analysisMunc18-1Syntaxin-1Polybasic regionTomosynSNAP-25Membrane fusionSynaptic vesiclesSingle-molecule force measurementsEssential intermediateSnareMotifInhibitory functionAssemblyMouse modelMunc18Synaptic transmissionSynaptic strength
2023
Roles for diacylglycerol in synaptic vesicle priming and release revealed by complete reconstitution of core protein machinery
Sundaram R, Chatterjee A, Bera M, Grushin K, Panda A, Li F, Coleman J, Lee S, Ramakrishnan S, Ernst A, Gupta K, Rothman J, Krishnakumar S. Roles for diacylglycerol in synaptic vesicle priming and release revealed by complete reconstitution of core protein machinery. Proceedings Of The National Academy Of Sciences Of The United States Of America 2023, 120: e2309516120. PMID: 37590407, PMCID: PMC10450444, DOI: 10.1073/pnas.2309516120.Peer-Reviewed Original ResearchConceptsCore protein machineryRelease-ready vesiclesSynaptic vesicle primingVesicle primingProtein machinerySingle-molecule imagingSNAREpin assemblyFunctional intermediatesFunctional reconstitutionMunc13DiacylglycerolCoordinated actionMunc18VesiclesMachineryComplete reconstitutionNew roleSelective effectDetailed characterizationChaperonesRate of caReconstitutionVAMP2ComplexinMutations
2015
Munc18‐2 is required for Syntaxin 11 Localization on the Plasma Membrane in Cytotoxic T‐Lymphocytes
Dieckmann N, Hackmann Y, Aricò M, Griffiths G. Munc18‐2 is required for Syntaxin 11 Localization on the Plasma Membrane in Cytotoxic T‐Lymphocytes. Traffic 2015, 16: 1330-1341. PMID: 26771955, PMCID: PMC4791091, DOI: 10.1111/tra.12337.Peer-Reviewed Original ResearchConceptsCytotoxic T lymphocytesPlasma membraneMunc18-2Granule secretionT lymphocytesMunc18Syntaxin-11Fusion eventsFamilial haemophagocytic lymphohistiocytosisEndogenous localizationSyntaxinImmunological synapseSTX11Cytolytic granulesFHL4Loss of proteinHaemophagocytic lymphohistiocytosisPrimary immunodeficiencyProteinFHL5MembraneSecretionPlasmaLocalizationCytotoxicity
2013
Syntaxin binding mechanism and disease-causing mutations in Munc18-2
Hackmann Y, Graham S, Ehl S, Höning S, Lehmberg K, Aricò M, Owen D, Griffiths G. Syntaxin binding mechanism and disease-causing mutations in Munc18-2. Proceedings Of The National Academy Of Sciences Of The United States Of America 2013, 110: e4482-e4491. PMID: 24194549, PMCID: PMC3839780, DOI: 10.1073/pnas.1313474110.Peer-Reviewed Original ResearchConceptsProtein receptor binding sitesDisease-causing mutationsN-terminal peptideCytotoxic T lymphocytesMunc18-2Munc18Syntaxin-11Surface mutationsSyntaxinA-resolutionSTX11Natural killer cellsMolecular mechanismsReceptor binding sitesBinding sitesMutationsIL-2 activitySTX3Higher affinityBinding mechanismIn vitro IL-2 activationIL-2-activated cellsFamilial hemophagocytic lymphohistiocytosisBindingSelective binding
2000
Mints as Adaptors DIRECT BINDING TO NEUREXINS AND RECRUITMENT OF Munc18*
Biederer T, Südhof T. Mints as Adaptors DIRECT BINDING TO NEUREXINS AND RECRUITMENT OF Munc18*. Journal Of Biological Chemistry 2000, 275: 39803-39806. PMID: 11036064, DOI: 10.1074/jbc.c000656200.Peer-Reviewed Original ResearchConceptsAdaptor proteinPDZ domain-mediated interactionsDomain-mediated interactionsSynaptic vesicle exocytosisCell surface proteinsNeuronal adaptor proteinMultiprotein complexesProtein essentialCytoplasmic tailMunc18-1Vesicle exocytosisPlasma membraneMunc18NeurexinsDirect bindingPossible functionsSurface proteinsProteinExocytosisMINT1RecruitmentComplexesMint2BindsMint
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